Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase
A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Published: |
Cambridge University Press
2016
|
| Subjects: | |
| Online Access: | https://eprints.nottingham.ac.uk/31612/ |
| _version_ | 1848794236071182336 |
|---|---|
| author | Igetei, Joseph E. Liddell, Susan El-Faham, Marwa Doenhoff, Michael J. |
| author_facet | Igetei, Joseph E. Liddell, Susan El-Faham, Marwa Doenhoff, Michael J. |
| author_sort | Igetei, Joseph E. |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion. |
| first_indexed | 2025-11-14T19:12:59Z |
| format | Article |
| id | nottingham-31612 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:12:59Z |
| publishDate | 2016 |
| publisher | Cambridge University Press |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-316122020-05-04T17:38:52Z https://eprints.nottingham.ac.uk/31612/ Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase Igetei, Joseph E. Liddell, Susan El-Faham, Marwa Doenhoff, Michael J. A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion. Cambridge University Press 2016-04-01 Article PeerReviewed Igetei, Joseph E., Liddell, Susan, El-Faham, Marwa and Doenhoff, Michael J. (2016) Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase. Parasitology, 143 (5). pp. 646-657. ISSN 1469-8161 S. mansoni host-derived enzyme mice carboxylesterase 1C immune evasion http://dx.doi.org/10.1017/S0031182016000184 doi:10.1017/S0031182016000184 doi:10.1017/S0031182016000184 |
| spellingShingle | S. mansoni host-derived enzyme mice carboxylesterase 1C immune evasion Igetei, Joseph E. Liddell, Susan El-Faham, Marwa Doenhoff, Michael J. Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
| title | Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
| title_full | Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
| title_fullStr | Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
| title_full_unstemmed | Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
| title_short | Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
| title_sort | purification of a chymotrypsin-like enzyme present on adult schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
| topic | S. mansoni host-derived enzyme mice carboxylesterase 1C immune evasion |
| url | https://eprints.nottingham.ac.uk/31612/ https://eprints.nottingham.ac.uk/31612/ https://eprints.nottingham.ac.uk/31612/ |